Pharmaceutical Sciences Faculty Publications

Title

NMR Study of the Positions of His-12 and His-119 in the Ribonuclease A-Uridine Vanadate Complex

Document Type

Article

Publication Date

7-1-1994

Journal Title

Biophysical Journal

ISSN

0006-3495

Volume

67

Issue

1

First Page

331

Last Page

335

DOI

10.1016/S0006-3495(94)80485-0

PubMed ID

7919003

PubMed Central® ID

PMC1225363

Abstract

The binding of uridine vanadate to ribonuclease A has been investigated by one- and two-dimensional 1H NMR. The homonuclear Nuclear Overhauser and exchange spectroscopy spectrum of the uridine vanadate/RNase A complex exhibits cross peaks between both the C5H and C6H protons of uridine vanadate and the H epsilon 1 proton of His-12 of ribonuclease A. These cross peaks suggest that the H epsilon 1 proton of His-12 is in the vicinity of the uracil base of uridine vanadate, as observed in the crystallographic structure of the uridine vanadate/RNase A complex. However, no cross peaks are observed between the C5H and C6H protons of uridine vanadate and the H epsilon 1 proton of His-119 of ribonuclease A, although they were predicted based upon the distances calculated from coordinates of the crystallographic structure of the complex. These results suggest that there is a significant difference between the positioning of the His-119 side chain in the solution and in the crystallographic structures.

Keywords

Amino acid sequence, binding sites, histidine, magnetic resonance spectroscopy, protein conformation, ribonuclease, pancreatic, uridine, vanadates

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